1dbd: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:1dbd.jpg|left|200px]]
{{Seed}}
[[Image:1dbd.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1dbd|  PDB=1dbd  |  SCENE=  }}  
{{STRUCTURE_1dbd|  PDB=1dbd  |  SCENE=  }}  


'''E2 DNA-BINDING DOMAIN FROM PAPILLOMAVIRUS BPV-1'''
===E2 DNA-BINDING DOMAIN FROM PAPILLOMAVIRUS BPV-1===




==Overview==
<!--  
Papillomaviral E2 proteins participate in viral DNA replication and transcriptional regulation. We have solved the solution structure of the DNA-binding domain of the E2 protein from bovine papillomavirus (BPV-1). The structure calculation used 2222 distance and 158 dihedral angle restraints for the homodimer (202 residues in total), which were derived from homonuclear and heteronuclear multidimensional nuclear magnetic resonance (NMR) spectroscopic data. The root-mean-square deviation for structured regions of the monomer when superimposed to the average is 0.73 +/- 0.10 A for backbone atoms and 1.42 +/- 0.16 A for heavy atoms. The 101 residue construct used in this study (residues 310-410) is about 4.5 kcal/mol more stable than a minimal domain comprising the C-terminal 85 amino acid residues (residues 326-410). The structure of the core domain contained within BPV-1 E2 is similar to the corresponding regions of other papilloma viral E2 proteins. Here, however, the extra N-terminal 16 residues form a flap that covers a cavity at the dimer interface and play a role in DNA binding. Interactions between residues in the N-terminal extension and the core domain correlate with the greater stability of the longer form of the protein relative to the minimal domain.
The line below this paragraph, {{ABSTRACT_PUBMED_10587434}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10587434 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_10587434}}


==About this Structure==
==About this Structure==
1DBD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bovine_papillomavirus_type_1 Bovine papillomavirus type 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DBD OCA].  
1DBD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bovine_papillomavirus_type_1 Bovine papillomavirus type 1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DBD OCA].  


==Reference==
==Reference==
Line 27: Line 31:
[[Category: Veeraraghavan, S.]]
[[Category: Veeraraghavan, S.]]
[[Category: Dna-binding domain]]
[[Category: Dna-binding domain]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:39:21 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:46:37 2008''

Revision as of 19:46, 30 June 2008

File:1dbd.png

Template:STRUCTURE 1dbd

E2 DNA-BINDING DOMAIN FROM PAPILLOMAVIRUS BPV-1

Template:ABSTRACT PUBMED 10587434

About this Structure

1DBD is a Single protein structure of sequence from Bovine papillomavirus type 1. Full experimental information is available from OCA.

Reference

Structural correlates for enhanced stability in the E2 DNA-binding domain from bovine papillomavirus., Veeraraghavan S, Mello CC, Androphy EJ, Baleja JD, Biochemistry. 1999 Dec 7;38(49):16115-24. PMID:10587434

Page seeded by OCA on Mon Jun 30 22:46:37 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1dbd&oldid=586615"